Abstract
Nuclear poly(A) polymerase (PAP) polyadenylates nascent mRNAs, promoting their nuclear export, stability, and translation, while the related cytoplasmic polymerase GLD-2 activates translation of deadenylated mRNAs. Here we characterize the biochemical activity of fission yeast Schizosaccharomyces pombe Cid1, a putative cytoplasmic PAP implicated in cell cycle checkpoint controls. Surprisingly, Cid1 has robust poly(U) polymerase activity in vitro, especially when isolated in native multiprotein complexes. Furthermore, we found that upon S-phase arrest, the 3' ends of actin mRNAs were posttranscriptionally uridylated in a Cid1-dependent manner. Finally, Hs2 (ZCCHC6), a human ortholog of Cid1, shows similar activity. These data suggest that uridylation of mRNA forms the basis of an evolutionarily conserved mechanism of gene regulation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actins / genetics
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Actins / metabolism
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Adenosine Triphosphate / metabolism
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Base Sequence
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Cell Cycle / physiology
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Humans
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Molecular Sequence Data
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Multienzyme Complexes
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Nucleotidyltransferases / genetics
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Nucleotidyltransferases / metabolism*
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Poly A / metabolism*
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Polynucleotide Adenylyltransferase / genetics
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Polynucleotide Adenylyltransferase / metabolism*
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RNA, Messenger / chemistry
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RNA, Messenger / metabolism*
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Schizosaccharomyces / genetics
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Schizosaccharomyces / metabolism
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Schizosaccharomyces pombe Proteins / genetics
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Schizosaccharomyces pombe Proteins / metabolism*
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Uridine Monophosphate / metabolism*
Substances
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Actins
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Multienzyme Complexes
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RNA, Messenger
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Recombinant Proteins
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Schizosaccharomyces pombe Proteins
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Poly A
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Adenosine Triphosphate
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Uridine Monophosphate
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Nucleotidyltransferases
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Cid1 protein, S pombe
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Polynucleotide Adenylyltransferase